ID A0A098UEZ9_9BURK Unreviewed; 1010 AA.
AC A0A098UEZ9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Gluconolaconase {ECO:0000313|EMBL:KGF81513.1};
GN ORFNames=IA69_12780 {ECO:0000313|EMBL:KGF81513.1};
OS Massilia sp. JS1662.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1519190 {ECO:0000313|EMBL:KGF81513.1, ECO:0000313|Proteomes:UP000029701};
RN [1] {ECO:0000313|EMBL:KGF81513.1, ECO:0000313|Proteomes:UP000029701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1662 {ECO:0000313|EMBL:KGF81513.1,
RC ECO:0000313|Proteomes:UP000029701};
RA Fida T.T., Spain J.C.;
RT "Identification of Arachidin-3 degrading bacteria in the peanut
RT rhizosphere.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGF81513.1}.
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DR EMBL; JPQD01000011; KGF81513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A098UEZ9; -.
DR OrthoDB; 241638at2; -.
DR Proteomes; UP000029701; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR013658; SGL.
DR PANTHER; PTHR47572:SF4; LACTONASE DRP35; 1.
DR PANTHER; PTHR47572; LIPOPROTEIN-RELATED; 1.
DR Pfam; PF12708; Pectate_lyase_3; 2.
DR Pfam; PF08450; SGL; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1010
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001941650"
FT DOMAIN 47..271
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
FT DOMAIN 384..437
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
FT DOMAIN 948..1001
FT /note="SMP-30/Gluconolactonase/LRE-like region"
FT /evidence="ECO:0000259|Pfam:PF08450"
SQ SEQUENCE 1010 AA; 109471 MW; 97DE6BB0A7F133CC CRC64;
MKTTLSTLLR PLPAALALAF VLAAPASAAS VSAFQTMPED PRAVVVHAKG DGKMDDTAAI
QQAIDAAANK GEGGVVFLPS GRYRITKSIL IPLAVRVYGV GATRPVFVLA PKTPGFQQGV
ANMVIFTGGD QYTVGKVPMP VAGAVGADKD VRDANSATFY SVLSNVDFEI GDGNPAATGV
RMHTAQHSNL SHIDFHIGSG LAGVYHVGNI AYDLKFHGGR YGILAEKTSP AWQFTLVDAT
FDGQRDAAIR EHEAGLTLDN VDIRDTPVGI DIDRGYGDWL YAKNVRFENV AKAAVVISNE
DNVYTQIAFD HASAKNVPTF AKFRDSGKTL AGAGRAYEVT ELNYGMKVDQ LGTPGRFTTN
YKTGPISKAA PQRVLKALPP SKEWANVHKF GAKGDGRADD TAAIQKAIDS NRVVYLPQGF
YMVNDTIRMK PDTVIVGLHP GLTQLVLPNG SPLFQGVDTP KALLESARGG AGIVSGIGLA
TGEVNNRAVA LLWRAGEQSL VDDVRIQGGH GTRLYDGTRA DPYKKTDRWD TTAWWDRQYP
SVWVTDGGGG TFTGIWSPSG YAQAGFYVTN TKTPGRVYEL SAEHHIRNEI VLDGVENWSF
YAPQTEEEVR DGMDSVSLDI RNSKNILIAN YHGYRVTRSI KPAVTAVRIA NSSDIRFRNV
HVNGESGFAT CDENGCTTYL RASKYPYENA ITDVTHNIEV REREFAILDY TGKQAAAPAP
SGKVEKVADG FYSVAGAAVD ANGKLYFIDR HFKRIHAWSR DRGLEIVRDT PLDPINLAID
RSGNVMVVSH YGPSASVYAF KPDVPPTPDG YTMIKPTAVA SRADARVAIP VNFWQNGEFQ
DQIDPKTYEF TTLSEMFARD VAKPKAQEYV SPDGSLVLPA WRVTRQGPTD HLGYRWSDTL
DTHGFTSARV GERVIFTNGS ENRTFSGLVG QGGAITDLKQ VADRGGESAT LGPDGNVYVA
NGQVFIYGPD GKERGRIDVP ERPLQLIFGG ADKRTLFILT HHALYTSHVD
//